Evidence map›Paper›PMID 30355441›Full record

ArticleeLife2018

Structures of translationally inactive mammalian ribosomes.

Alan Brown, Matthew R Baird, Matthew Cj Yip, Jason Murray, Sichen Shao

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
3.8field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

92 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
  2. Article
  3. eLife · 2026
    Article
  4. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. A ribosomal kinetic checkpoint governs selective mRNA recruitment.bioRxiv : the preprint server for biology · 2026
    Article
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32 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Alan BrownDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States.ORCID http://orcid.org/0000-0002-0021-0476
Matthew R BairdDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States.
Matthew Cj YipDepartment of Cell Biology, Harvard Medical School, Boston, United States.ORCID http://orcid.org/0000-0002-2505-9987
Jason MurrayMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-8679-8281
Sichen ShaoDepartment of Cell Biology, Harvard Medical School, Boston, United States.ORCID http://orcid.org/0000-0003-2679-5537
Harvard University · USMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184332
6 · The paper itself

Abstract

The cellular levels and activities of ribosomes directly regulate gene expression during numerous physiological processes. The mechanisms that globally repress translation are incompletely understood. Here, we use electron cryomicroscopy to analyze inactive ribosomes isolated from mammalian reticulocytes, the penultimate stage of red blood cell differentiation. We identify two types of ribosomes that are translationally repressed by protein interactions. The first comprises ribosomes sequestered with elongation factor 2 (eEF2) by SERPINE mRNA binding protein 1 (SERBP1) occupying the ribosomal mRNA entrance channel. The second type are translationally repressed by a novel ribosome-binding protein, interferon-related developmental regulator 2 (IFRD2), which spans the P and E sites and inserts a C-terminal helix into the mRNA exit channel to preclude translation. IFRD2 binds ribosomes with a tRNA occupying a noncanonical binding site, the 'Z site', on the ribosome. These structures provide functional insights into how ribosomal interactions may suppress translation to regulate gene expression.

Indexed as

Protein BiosynthesisAmino Acid SequenceAnimalsBinding SitesHEK293 CellsHumansMammalsMembrane ProteinsModels, MolecularMolecular ConformationPeptide Elongation Factor 2Protein BindingRabbitsReticulocytesRibosomesRNA-Binding ProteinsMembrane ProteinsPeptide Elongation Factor 2RNA-Binding ProteinsRNA, Transferelectron cryomicroscopyin vitro reconstitutionmolecular biophysicsnoneribosomestructural biology

Identifiers

PMID30355441
PMCPMC6226290
OpenAlexW2898235321

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.